ID   KAR3_YEAST              Reviewed;         729 AA.
AC   P17119; D6W4D9;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   27-MAR-2024, entry version 218.
DE   RecName: Full=Kinesin-like protein KAR3;
DE            EC=5.6.1.4 {ECO:0000269|PubMed:17382884, ECO:0000269|PubMed:22734002, ECO:0000269|PubMed:25313961, ECO:0000305|PubMed:11387196, ECO:0000305|PubMed:9859995};
DE   AltName: Full=Nuclear fusion protein;
GN   Name=KAR3; OrderedLocusNames=YPR141C; ORFNames=P9659.16;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC   STRAIN=MY1124;
RX   PubMed=2138512; DOI=10.1016/0092-8674(90)90351-e;
RA   Meluh P.B., Rose M.D.;
RT   "KAR3, a kinesin-related gene required for yeast nuclear fusion.";
RL   Cell 60:1029-1041(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169875;
RA   Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA   Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA   Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA   Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA   DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA   Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA   Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA   Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA   Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA   Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA   Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA   Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA   Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA   Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA   Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA   Vo D.H., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL   Nature 387:103-105(1997).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   FUNCTION.
RX   PubMed=8224825; DOI=10.1093/genetics/135.1.35;
RA   Hoyt M.A., He L., Totis L., Saunders W.S.;
RT   "Loss of function of Saccharomyces cerevisiae kinesin-related CIN8 and KIP1
RT   is suppressed by KAR3 motor domain mutations.";
RL   Genetics 135:35-44(1993).
RN   [5]
RP   FUNCTION.
RX   PubMed=7912193; DOI=10.1002/j.1460-2075.1994.tb06561.x;
RA   Endow S.A., Kang S.J., Satterwhite L.L., Rose M.D., Skeen V.P.,
RA   Salmon E.D.;
RT   "Yeast Kar3 is a minus-end microtubule motor protein that destabilizes
RT   microtubules preferentially at the minus ends.";
RL   EMBO J. 13:2708-2713(1994).
RN   [6]
RP   FUNCTION, INTERACTION WITH CIK1, AND DISRUPTION PHENOTYPE.
RX   PubMed=8106549; DOI=10.1083/jcb.124.4.507;
RA   Page B.D., Satterwhite L.L., Rose M.D., Snyder M.;
RT   "Localization of the Kar3 kinesin heavy chain-related protein requires the
RT   Cik1 interacting protein.";
RL   J. Cell Biol. 124:507-519(1994).
RN   [7]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=9334348; DOI=10.1083/jcb.139.2.459;
RA   Bascom-Slack C.A., Dawson D.S.;
RT   "The yeast motor protein, Kar3p, is essential for meiosis I.";
RL   J. Cell Biol. 139:459-467(1997).
RN   [8]
RP   FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF ASN-650.
RX   PubMed=9859995; DOI=10.1038/25153;
RA   Song H., Endow S.A.;
RT   "Decoupling of nucleotide- and microtubule-binding sites in a kinesin
RT   mutant.";
RL   Nature 396:587-590(1998).
RN   [9]
RP   FUNCTION, INTERACTION WITH CIK1 AND VIK1, AND SUBCELLULAR LOCATION.
RX   PubMed=10087265; DOI=10.1083/jcb.144.6.1219;
RA   Manning B.D., Barrett J.G., Wallace J.A., Granok H., Snyder M.;
RT   "Differential regulation of the Kar3p kinesin-related protein by two
RT   associated proteins, Cik1p and Vik1p.";
RL   J. Cell Biol. 144:1219-1233(1999).
RN   [10]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=11729143; DOI=10.1093/genetics/159.3.939;
RA   Shanks R.M.Q., Kamieniecki R.J., Dawson D.S.;
RT   "The Kar3-interacting protein Cik1p plays a critical role in passage
RT   through meiosis I in Saccharomyces cerevisiae.";
RL   Genetics 159:939-951(2001).
RN   [11]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [12]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, INTERACTION
RP   WITH VIK1 AND CIK1, AND SUBCELLULAR LOCATION.
RX   PubMed=17382884; DOI=10.1016/j.cell.2006.12.046;
RA   Allingham J.S., Sproul L.R., Rayment I., Gilbert S.P.;
RT   "Vik1 modulates microtubule-Kar3 interactions through a motor domain that
RT   lacks an active site.";
RL   Cell 128:1161-1172(2007).
RN   [13]
RP   FUNCTION.
RX   PubMed=18079178; DOI=10.1101/gad.449407;
RA   Kitamura E., Tanaka K., Kitamura Y., Tanaka T.U.;
RT   "Kinetochore microtubule interaction during S phase in Saccharomyces
RT   cerevisiae.";
RL   Genes Dev. 21:3319-3330(2007).
RN   [14]
RP   FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX   PubMed=15846338; DOI=10.1038/nature03483;
RA   Tanaka K., Mukae N., Dewar H., van Breugel M., James E.K., Prescott A.R.,
RA   Antony C., Tanaka T.U.;
RT   "Molecular mechanisms of kinetochore capture by spindle microtubules.";
RL   Nature 434:987-994(2005).
RN   [15]
RP   FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX   PubMed=17620411; DOI=10.1083/jcb.200702141;
RA   Tanaka K., Kitamura E., Kitamura Y., Tanaka T.U.;
RT   "Molecular mechanisms of microtubule-dependent kinetochore transport toward
RT   spindle poles.";
RL   J. Cell Biol. 178:269-281(2007).
RN   [16]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=25313961; DOI=10.1016/j.devcel.2014.07.023;
RA   Hepperla A.J., Willey P.T., Coombes C.E., Schuster B.M., Gerami-Nejad M.,
RA   McClellan M., Mukherjee S., Fox J., Winey M., Odde D.J., O'Toole E.,
RA   Gardner M.K.;
RT   "Minus-end-directed Kinesin-14 motors align antiparallel microtubules to
RT   control metaphase spindle length.";
RL   Dev. Cell 31:61-72(2014).
RN   [17] {ECO:0007744|PDB:3KAR}
RP   X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 383-729 IN COMPLEX WITH ADP, AND
RP   ATP-BINDING.
RX   PubMed=9485302; DOI=10.1021/bi972504o;
RA   Gulick A.M., Song H., Endow S.A., Rayment I.;
RT   "X-ray crystal structure of the yeast Kar3 motor domain complexed with
RT   Mg.ADP to 2.3-A resolution.";
RL   Biochemistry 37:1769-1776(1998).
RN   [18] {ECO:0007744|PDB:1F9T, ECO:0007744|PDB:1F9U, ECO:0007744|PDB:1F9V, ECO:0007744|PDB:1F9W}
RP   X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) OF 384-729 IN COMPLEX WITH ADP,
RP   FUNCTION, CATALYTIC ACTIVITY, ATP-BINDING, AND MUTAGENESIS OF ARG-598;
RP   GLU-631 AND ARG-632.
RX   PubMed=11387196; DOI=10.1093/emboj/20.11.2611;
RA   Yun M., Zhang X., Park C.G., Park H.W., Endow S.A.;
RT   "A structural pathway for activation of the kinesin motor ATPase.";
RL   EMBO J. 20:2611-2618(2001).
RN   [19] {ECO:0007744|PDB:4ETP}
RP   X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 331-729 IN COMPLEX WITH VIK1 AND
RP   ADP, FUNCTION, CATALYTIC ACTIVITY, AND ATP-BINDING.
RX   PubMed=22734002; DOI=10.1083/jcb.201201132;
RA   Rank K.C., Chen C.J., Cope J., Porche K., Hoenger A., Gilbert S.P.,
RA   Rayment I.;
RT   "Kar3Vik1, a member of the kinesin-14 superfamily, shows a novel kinesin
RT   microtubule binding pattern.";
RL   J. Cell Biol. 197:957-970(2012).
CC   -!- FUNCTION: Minus end-directed microtubule (MT) motor involved in spindle
CC       midzone assembly, poleward transport of newly captured kinetochores
CC       along the lateral side of MTs, karyogamy (nuclear fusion) during
CC       mating, and with an essential function in meiosis I (PubMed:7912193,
CC       PubMed:8106549, PubMed:9334348, PubMed:9859995, PubMed:11729143,
CC       PubMed:17382884, PubMed:17620411, PubMed:25313961, PubMed:11387196,
CC       PubMed:22734002). Functions together with the accessory proteins CIK1
CC       or VIK1 (PubMed:10087265, PubMed:11729143, PubMed:17382884,
CC       PubMed:15846338, PubMed:25313961, PubMed:22734002). Drives the poleward
CC       transport of newly captured kinetochores along the lateral side of MTs,
CC       both during S-phase and during M-phase (PubMed:18079178,
CC       PubMed:15846338, PubMed:17620411). To contribute to spindle midzone
CC       assembly during mitotic metaphase, the nuclear KAR3-CIK1 motor cross-
CC       links anti-parallel microtubules to align them on the spindle axis; as
CC       the motor travels polewards splayed microtubules are pulled into
CC       alignment (PubMed:25313961). During the karyogamy (nuclear fusion) step
CC       of mating, KAR3-CIK1 cross-links antiparallel cytoplasmic microtubules
CC       emanating from the spindle pole bodies of mating partners; the motor
CC       activity of KAR3 creates the force that pulls the nuclei together by
CC       sliding cross-linked microtubules past one another (PubMed:2138512,
CC       PubMed:8106549). KAR3-CIK1 promotes microtubule shortening
CC       predominantly from the microtubule plus-end (PubMed:17382884). Together
CC       with cytoplasmic VIK1, may act to stabilize microtubules
CC       (PubMed:17382884). Requires accessory protein VIK1 for spindle pole
CC       body localization and to allow the CIN8 and KIP1 motors to generate
CC       outwardly directed spindle forces (PubMed:2138512, PubMed:8224825,
CC       PubMed:7912193, PubMed:11729143). Essential during meiosis I
CC       (PubMed:9334348). The ATPase activity is stimulated by microtubule-
CC       binding (PubMed:9859995, PubMed:11387196, PubMed:22734002).
CC       {ECO:0000269|PubMed:10087265, ECO:0000269|PubMed:11387196,
CC       ECO:0000269|PubMed:11729143, ECO:0000269|PubMed:15846338,
CC       ECO:0000269|PubMed:17382884, ECO:0000269|PubMed:17620411,
CC       ECO:0000269|PubMed:18079178, ECO:0000269|PubMed:2138512,
CC       ECO:0000269|PubMed:22734002, ECO:0000269|PubMed:25313961,
CC       ECO:0000269|PubMed:7912193, ECO:0000269|PubMed:8106549,
CC       ECO:0000269|PubMed:8224825, ECO:0000269|PubMed:9334348,
CC       ECO:0000269|PubMed:9859995}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000269|PubMed:11387196, ECO:0000269|PubMed:17382884,
CC         ECO:0000269|PubMed:22734002, ECO:0000269|PubMed:9859995};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC         Evidence={ECO:0000269|PubMed:11387196, ECO:0000269|PubMed:17382884,
CC         ECO:0000269|PubMed:22734002, ECO:0000269|PubMed:9859995};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + a kinesin associated with a microtubule at
CC         position (n) = ADP + phosphate + a kinesin associated with a
CC         microtubule at position (n-1, toward the minus end).; EC=5.6.1.4;
CC         Evidence={ECO:0000269|PubMed:17382884, ECO:0000269|PubMed:22734002,
CC         ECO:0000269|PubMed:25313961, ECO:0000305|PubMed:11387196,
CC         ECO:0000305|PubMed:9859995};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=12.2 uM for MgATP {ECO:0000269|PubMed:17382884};
CC         KM=18.6 uM for MgATP in complex with CIK1
CC         {ECO:0000269|PubMed:17382884};
CC         KM=15 uM for MgATP in complex with VIK1
CC         {ECO:0000269|PubMed:17382884};
CC         Note=kcat is 0.49 sec(-1) with MgATP as substrate (PubMed:17382884).
CC         kcat is 2.8 sec(-1) with MgATP as substrate in complex with CIK1
CC         (PubMed:17382884). kcat is 3.7 sec(-1) with MgATP as substrate in
CC         complex with VIK1 (PubMed:17382884). {ECO:0000269|PubMed:17382884};
CC   -!- SUBUNIT: Interacts with CIK1; the interaction is direct
CC       (PubMed:8106549, PubMed:10087265, PubMed:17382884). Interacts with
CC       VIK1; the interaction is direct (PubMed:10087265, PubMed:17382884).
CC       {ECO:0000269|PubMed:10087265, ECO:0000269|PubMed:17382884,
CC       ECO:0000269|PubMed:8106549}.
CC   -!- INTERACTION:
CC       P17119; P32908: SMC1; NbExp=4; IntAct=EBI-9499, EBI-17402;
CC       P17119; Q12045: VIK1; NbExp=4; IntAct=EBI-9499, EBI-38784;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC       center, spindle pole body {ECO:0000269|PubMed:10087265,
CC       ECO:0000269|PubMed:11729143, ECO:0000269|PubMed:25313961}. Nucleus
CC       {ECO:0000269|PubMed:11729143, ECO:0000269|PubMed:17620411}. Cytoplasm,
CC       cytoskeleton {ECO:0000269|PubMed:11729143, ECO:0000269|PubMed:17382884,
CC       ECO:0000269|PubMed:17620411, ECO:0000269|PubMed:25313961}. Chromosome
CC       {ECO:0000269|PubMed:15846338}. Cytoplasm, cytoskeleton, spindle
CC       {ECO:0000269|PubMed:17620411, ECO:0000269|PubMed:25313961}.
CC       Note=Cytoplasmic microtubules. {ECO:0000269|PubMed:2138512}.
CC   -!- INDUCTION: By alpha factor.
CC   -!- DISRUPTION PHENOTYPE: Short mitotic metaphase spindles with splayed
CC       microtubules (MTs) increasing spindle width (PubMed:25313961). Disrupts
CC       the poleward movement of kinetochores on MTs; abolishes poleward
CC       sliding along the lateral side of MTs and increases end-on pulling
CC       (PubMed:17620411, PubMed:15846338). During karyogamy, (the mating step
CC       where nuclei fuse), abolishes the formation of a MT bridge between the
CC       two nuclei thereby leading to a failure in nuclear fusion
CC       (PubMed:8106549). Abnormal meiosis I; cells do not progress past
CC       prophase I, interhomolog recombination is abnormal and the organization
CC       of MTs is abnormal (PubMed:9334348). {ECO:0000269|PubMed:15846338,
CC       ECO:0000269|PubMed:17620411, ECO:0000269|PubMed:25313961,
CC       ECO:0000269|PubMed:8106549, ECO:0000269|PubMed:9334348}.
CC   -!- MISCELLANEOUS: KAR3 contains two globular domains separated by an
CC       alpha-helical coiled coil. The N-terminal portion of KAR3 contains a
CC       microtubule association domain distinct from the kinesin-like C-
CC       terminal domain.
CC   -!- MISCELLANEOUS: Present with 3250 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Kinesin family. NCD subfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU00283}.
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DR   EMBL; M31719; AAA34715.1; -; mRNA.
DR   EMBL; U40829; AAB68281.1; -; Genomic_DNA.
DR   EMBL; BK006949; DAA11555.1; -; Genomic_DNA.
DR   PIR; A34796; A34796.
DR   RefSeq; NP_015467.1; NM_001184238.1.
DR   PDB; 1F9T; X-ray; 1.50 A; A=372-729.
DR   PDB; 1F9U; X-ray; 1.70 A; A=383-729.
DR   PDB; 1F9V; X-ray; 1.30 A; A=383-729.
DR   PDB; 1F9W; X-ray; 2.50 A; A/B=383-729.
DR   PDB; 3KAR; X-ray; 2.30 A; A=385-729.
DR   PDB; 4ETP; X-ray; 2.30 A; A=348-729.
DR   PDBsum; 1F9T; -.
DR   PDBsum; 1F9U; -.
DR   PDBsum; 1F9V; -.
DR   PDBsum; 1F9W; -.
DR   PDBsum; 3KAR; -.
DR   PDBsum; 4ETP; -.
DR   AlphaFoldDB; P17119; -.
DR   SMR; P17119; -.
DR   BioGRID; 36310; 639.
DR   DIP; DIP-75N; -.
DR   IntAct; P17119; 8.
DR   MINT; P17119; -.
DR   STRING; 4932.YPR141C; -.
DR   iPTMnet; P17119; -.
DR   MaxQB; P17119; -.
DR   PaxDb; 4932-YPR141C; -.
DR   PeptideAtlas; P17119; -.
DR   EnsemblFungi; YPR141C_mRNA; YPR141C; YPR141C.
DR   GeneID; 856263; -.
DR   KEGG; sce:YPR141C; -.
DR   AGR; SGD:S000006345; -.
DR   SGD; S000006345; KAR3.
DR   VEuPathDB; FungiDB:YPR141C; -.
DR   eggNOG; KOG0239; Eukaryota.
DR   GeneTree; ENSGT00940000154022; -.
DR   HOGENOM; CLU_001485_12_4_1; -.
DR   InParanoid; P17119; -.
DR   OMA; ETARDKW; -.
DR   OrthoDB; 5476186at2759; -.
DR   BioCyc; YEAST:G3O-34276-MONOMER; -.
DR   BRENDA; 5.6.1.4; 984.
DR   BioGRID-ORCS; 856263; 1 hit in 10 CRISPR screens.
DR   EvolutionaryTrace; P17119; -.
DR   PRO; PR:P17119; -.
DR   Proteomes; UP000002311; Chromosome XVI.
DR   RNAct; P17119; Protein.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005881; C:cytoplasmic microtubule; IDA:SGD.
DR   GO; GO:0005874; C:microtubule; HDA:SGD.
DR   GO; GO:0005634; C:nucleus; HDA:SGD.
DR   GO; GO:0000922; C:spindle pole; HDA:SGD.
DR   GO; GO:0005816; C:spindle pole body; IDA:SGD.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IDA:UniProtKB.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
DR   GO; GO:0008569; F:minus-end-directed microtubule motor activity; IDA:UniProtKB.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0000742; P:karyogamy involved in conjugation with cellular fusion; IMP:SGD.
DR   GO; GO:0051321; P:meiotic cell cycle; IDA:SGD.
DR   GO; GO:1903562; P:microtubule bundle formation involved in mitotic spindle midzone assembly; IDA:UniProtKB.
DR   GO; GO:0000278; P:mitotic cell cycle; IMP:SGD.
DR   GO; GO:0007064; P:mitotic sister chromatid cohesion; IMP:SGD.
DR   GO; GO:0000743; P:nuclear migration involved in conjugation with cellular fusion; IMP:SGD.
DR   GO; GO:1990976; P:protein transport along microtubule to mitotic spindle pole body; IMP:UniProtKB.
DR   GO; GO:0060236; P:regulation of mitotic spindle organization; IMP:SGD.
DR   CDD; cd01366; KISc_C_terminal; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR   InterPro; IPR027640; Kinesin-like_fam.
DR   InterPro; IPR019821; Kinesin_motor_CS.
DR   InterPro; IPR001752; Kinesin_motor_dom.
DR   InterPro; IPR036961; Kinesin_motor_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR47972; KINESIN-LIKE PROTEIN KLP-3; 1.
DR   PANTHER; PTHR47972:SF28; PROTEIN CLARET SEGREGATIONAL; 1.
DR   Pfam; PF00225; Kinesin; 1.
DR   PRINTS; PR00380; KINESINHEAVY.
DR   SMART; SM00129; KISc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR   PROSITE; PS50067; KINESIN_MOTOR_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Cell cycle; Cell division; Chromosome;
KW   Coiled coil; Cytoplasm; Cytoskeleton; Isomerase; Karyogamy; Microtubule;
KW   Motor protein; Nucleotide-binding; Nucleus; Reference proteome.
FT   CHAIN           1..729
FT                   /note="Kinesin-like protein KAR3"
FT                   /id="PRO_0000125391"
FT   DOMAIN          386..723
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT   REGION          1..109
FT                   /note="Globular"
FT   REGION          1..48
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          110..357
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1..45
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         386
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000269|PubMed:11387196,
FT                   ECO:0007744|PDB:1F9V"
FT   BINDING         388
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000269|PubMed:11387196,
FT                   ECO:0007744|PDB:1F9V"
FT   BINDING         392
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000269|PubMed:11387196,
FT                   ECO:0000269|PubMed:22734002, ECO:0000269|PubMed:9485302,
FT                   ECO:0007744|PDB:1F9T, ECO:0007744|PDB:1F9U,
FT                   ECO:0007744|PDB:1F9V, ECO:0007744|PDB:1F9W,
FT                   ECO:0007744|PDB:3KAR, ECO:0007744|PDB:4ETP"
FT   BINDING         454
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000269|PubMed:11387196,
FT                   ECO:0007744|PDB:1F9V"
FT   BINDING         477
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000269|PubMed:11387196,
FT                   ECO:0000269|PubMed:22734002, ECO:0000269|PubMed:9485302,
FT                   ECO:0007744|PDB:1F9T, ECO:0007744|PDB:1F9U,
FT                   ECO:0007744|PDB:1F9V, ECO:0007744|PDB:1F9W,
FT                   ECO:0007744|PDB:3KAR, ECO:0007744|PDB:4ETP"
FT   BINDING         478
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000269|PubMed:11387196,
FT                   ECO:0007744|PDB:1F9W"
FT   BINDING         479
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000269|PubMed:11387196,
FT                   ECO:0000269|PubMed:22734002, ECO:0000269|PubMed:9485302,
FT                   ECO:0007744|PDB:1F9T, ECO:0007744|PDB:1F9U,
FT                   ECO:0007744|PDB:1F9V, ECO:0007744|PDB:1F9W,
FT                   ECO:0007744|PDB:3KAR, ECO:0007744|PDB:4ETP"
FT   BINDING         480
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000269|PubMed:11387196,
FT                   ECO:0000269|PubMed:22734002, ECO:0000269|PubMed:9485302,
FT                   ECO:0007744|PDB:1F9T, ECO:0007744|PDB:1F9U,
FT                   ECO:0007744|PDB:1F9V, ECO:0007744|PDB:1F9W,
FT                   ECO:0007744|PDB:3KAR, ECO:0007744|PDB:4ETP"
FT   BINDING         481
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000269|PubMed:11387196,
FT                   ECO:0000269|PubMed:22734002, ECO:0000269|PubMed:9485302,
FT                   ECO:0007744|PDB:1F9T, ECO:0007744|PDB:1F9U,
FT                   ECO:0007744|PDB:1F9V, ECO:0007744|PDB:1F9W,
FT                   ECO:0007744|PDB:3KAR, ECO:0007744|PDB:4ETP"
FT   BINDING         482
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000269|PubMed:11387196,
FT                   ECO:0000269|PubMed:22734002, ECO:0000269|PubMed:9485302,
FT                   ECO:0007744|PDB:1F9T, ECO:0007744|PDB:1F9U,
FT                   ECO:0007744|PDB:1F9V, ECO:0007744|PDB:1F9W,
FT                   ECO:0007744|PDB:3KAR, ECO:0007744|PDB:4ETP"
FT   BINDING         554
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000269|PubMed:22734002,
FT                   ECO:0007744|PDB:4ETP"
FT   BINDING         579
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000269|PubMed:11387196,
FT                   ECO:0007744|PDB:1F9V"
FT   BINDING         694
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000269|PubMed:11387196,
FT                   ECO:0007744|PDB:1F9V"
FT   VARIANT         378
FT                   /note="N -> K (in KAR3-894)"
FT   VARIANT         462
FT                   /note="S -> L (in KAR3-891)"
FT   VARIANT         521
FT                   /note="E -> D (in KAR3-893)"
FT   VARIANT         550
FT                   /note="R -> S (in KAR3-899)"
FT   VARIANT         558
FT                   /note="T -> A (in KAR3-8912)"
FT   VARIANT         650
FT                   /note="N -> K (in KAR3-898)"
FT   VARIANT         659
FT                   /note="V -> L (in KAR3-897)"
FT   MUTAGEN         479
FT                   /note="G->E: Poisons nuclear fusion."
FT   MUTAGEN         598
FT                   /note="R->A: Disrupts microtubule binding. Abolishes
FT                   microtubule-activated ATPase activity."
FT                   /evidence="ECO:0000269|PubMed:11387196"
FT   MUTAGEN         631
FT                   /note="E->A: Increases strength of microtubule binding.
FT                   Abolishes microtubule-activated ATPase activity."
FT                   /evidence="ECO:0000269|PubMed:11387196"
FT   MUTAGEN         632
FT                   /note="R->A: Decreases microtubule-activated ATPase
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:11387196"
FT   MUTAGEN         650
FT                   /note="N->K: Increases strength of microtubule binding.
FT                   Prevents release of ADP upon microtubule-binding."
FT                   /evidence="ECO:0000269|PubMed:9859995"
FT   HELIX           331..338
FT                   /evidence="ECO:0007829|PDB:4ETP"
FT   HELIX           340..384
FT                   /evidence="ECO:0007829|PDB:4ETP"
FT   STRAND          386..393
FT                   /evidence="ECO:0007829|PDB:1F9V"
FT   TURN            398..400
FT                   /evidence="ECO:0007829|PDB:1F9V"
FT   STRAND          406..410
FT                   /evidence="ECO:0007829|PDB:1F9V"
FT   TURN            415..418
FT                   /evidence="ECO:0007829|PDB:1F9V"
FT   STRAND          419..426
FT                   /evidence="ECO:0007829|PDB:1F9V"
FT   HELIX           427..429
FT                   /evidence="ECO:0007829|PDB:1F9V"
FT   STRAND          433..442
FT                   /evidence="ECO:0007829|PDB:1F9V"
FT   HELIX           448..459
FT                   /evidence="ECO:0007829|PDB:1F9V"
FT   HELIX           460..464
FT                   /evidence="ECO:0007829|PDB:1F9V"
FT   STRAND          468..473
FT                   /evidence="ECO:0007829|PDB:1F9V"
FT   HELIX           480..485
FT                   /evidence="ECO:0007829|PDB:1F9V"
FT   TURN            487..489
FT                   /evidence="ECO:0007829|PDB:1F9V"
FT   HELIX           491..506
FT                   /evidence="ECO:0007829|PDB:1F9V"
FT   HELIX           507..509
FT                   /evidence="ECO:0007829|PDB:1F9V"
FT   STRAND          512..523
FT                   /evidence="ECO:0007829|PDB:1F9V"
FT   STRAND          526..529
FT                   /evidence="ECO:0007829|PDB:1F9V"
FT   STRAND          549..552
FT                   /evidence="ECO:0007829|PDB:1F9V"
FT   TURN            553..556
FT                   /evidence="ECO:0007829|PDB:1F9V"
FT   STRAND          557..560
FT                   /evidence="ECO:0007829|PDB:1F9V"
FT   STRAND          566..570
FT                   /evidence="ECO:0007829|PDB:3KAR"
FT   HELIX           571..573
FT                   /evidence="ECO:0007829|PDB:1F9V"
FT   HELIX           574..581
FT                   /evidence="ECO:0007829|PDB:1F9V"
FT   HELIX           596..598
FT                   /evidence="ECO:0007829|PDB:1F9V"
FT   STRAND          599..610
FT                   /evidence="ECO:0007829|PDB:1F9V"
FT   TURN            612..614
FT                   /evidence="ECO:0007829|PDB:1F9U"
FT   STRAND          617..626
FT                   /evidence="ECO:0007829|PDB:1F9V"
FT   HELIX           635..637
FT                   /evidence="ECO:0007829|PDB:1F9V"
FT   HELIX           640..663
FT                   /evidence="ECO:0007829|PDB:1F9V"
FT   TURN            668..670
FT                   /evidence="ECO:0007829|PDB:4ETP"
FT   HELIX           675..677
FT                   /evidence="ECO:0007829|PDB:1F9V"
FT   HELIX           679..688
FT                   /evidence="ECO:0007829|PDB:1F9V"
FT   STRAND          693..700
FT                   /evidence="ECO:0007829|PDB:1F9V"
FT   HELIX           704..706
FT                   /evidence="ECO:0007829|PDB:1F9V"
FT   HELIX           707..720
FT                   /evidence="ECO:0007829|PDB:1F9V"
FT   TURN            723..725
FT                   /evidence="ECO:0007829|PDB:1F9V"
SQ   SEQUENCE   729 AA;  84004 MW;  BAEF98BC783ABDB9 CRC64;
     MESLPRTPTK GRSTQHLSTP SPKNDILAMN GHKRRNTTTP PPKHTLLKPQ RTDIHRHSLA
     SQSRISMSPN RELLKNYKGT ANLIYGNQKS NSGVTSFYKE NVNELNRTQA ILFEKKATLD
     LLKDELTETK EKINAVNLKF ETLREEKIKI EQQLNLKNNE LISIKEEFLS KKQFMNEGHE
     IHLKQLAASN KKELKQMENE YKTKIEKLKF MKIKQFENER ASLLDKIEEV RNKITMNPST
     LQEMLNDVEQ KHMLEKEEWL TEYQSQWKKD IELNNKHMQE IESIKKEIEN TLKPELAEKK
     KLLTEKRNAY EAIKVKVKEK EEETTRLRDE VALKQKTNLE TLEKIKELEE YIKDTELGMK
     ELNEILIKEE TVRRTLHNEL QELRGNIRVY CRIRPALKNL ENSDTSLINV NEFDDNSGVQ
     SMEVTKIQNT AQVHEFKFDK IFDQQDTNVD VFKEVGQLVQ SSLDGYNVCI FAYGQTGSGK
     TFTMLNPGDG IIPSTISHIF NWINKLKTKG WDYKVNCEFI EIYNENIVDL LRSDNNNKED
     TSIGLKHEIR HDQETKTTTI TNVTSCKLES EEMVEIILKK ANKLRSTAST ASNEHSSRSH
     SIFIIHLSGS NAKTGAHSYG TLNLVDLAGS ERINVSQVVG DRLRETQNIN KSLSCLGDVI
     HALGQPDSTK RHIPFRNSKL TYLLQYSLTG DSKTLMFVNI SPSSSHINET LNSLRFASKV
     NSTRLVSRK
//